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5D2M

Complex between human SUMO2-RANGAP1, UBC9 and ZNF451

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000166molecular_functionnucleotide binding
A0000795cellular_componentsynaptonemal complex
A0001221molecular_functiontranscription coregulator binding
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006511biological_processubiquitin-dependent protein catabolic process
A0007059biological_processchromosome segregation
A0007084biological_processmitotic nuclear membrane reassembly
A0008134molecular_functiontranscription factor binding
A0016604cellular_componentnuclear body
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0016925biological_processprotein sumoylation
A0019789molecular_functionSUMO transferase activity
A0019899molecular_functionenzyme binding
A0030335biological_processpositive regulation of cell migration
A0036211biological_processprotein modification process
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043398molecular_functionHLH domain binding
A0044388molecular_functionsmall protein activating enzyme binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0048471cellular_componentperinuclear region of cytoplasm
A0050804biological_processmodulation of chemical synaptic transmission
A0051168biological_processnuclear export
A0051301biological_processcell division
A0061656molecular_functionSUMO conjugating enzyme activity
A0071535molecular_functionRING-like zinc finger domain binding
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098978cellular_componentglutamatergic synapse
A0099523cellular_componentpresynaptic cytosol
A0099524cellular_componentpostsynaptic cytosol
A0106068cellular_componentSUMO ligase complex
A1990234cellular_componenttransferase complex
C0005096molecular_functionGTPase activator activity
C0007165biological_processsignal transduction
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000166molecular_functionnucleotide binding
D0000795cellular_componentsynaptonemal complex
D0001221molecular_functiontranscription coregulator binding
D0003723molecular_functionRNA binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006511biological_processubiquitin-dependent protein catabolic process
D0007059biological_processchromosome segregation
D0007084biological_processmitotic nuclear membrane reassembly
D0008134molecular_functiontranscription factor binding
D0016604cellular_componentnuclear body
D0016605cellular_componentPML body
D0016740molecular_functiontransferase activity
D0016925biological_processprotein sumoylation
D0019789molecular_functionSUMO transferase activity
D0019899molecular_functionenzyme binding
D0030335biological_processpositive regulation of cell migration
D0036211biological_processprotein modification process
D0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
D0043398molecular_functionHLH domain binding
D0044388molecular_functionsmall protein activating enzyme binding
D0045892biological_processnegative regulation of DNA-templated transcription
D0048471cellular_componentperinuclear region of cytoplasm
D0050804biological_processmodulation of chemical synaptic transmission
D0051168biological_processnuclear export
D0051301biological_processcell division
D0061656molecular_functionSUMO conjugating enzyme activity
D0071535molecular_functionRING-like zinc finger domain binding
D0098685cellular_componentSchaffer collateral - CA1 synapse
D0098978cellular_componentglutamatergic synapse
D0099523cellular_componentpresynaptic cytosol
D0099524cellular_componentpostsynaptic cytosol
D0106068cellular_componentSUMO ligase complex
D1990234cellular_componenttransferase complex
F0005096molecular_functionGTPase activator activity
F0007165biological_processsignal transduction
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue EDO A 301
ChainResidue
ALYS18
AASP19
AHOH432
AHOH434
AHOH471
ETHR83
GARG40

site_idAC2
Number of Residues1
Detailsbinding site for residue EDO C 601
ChainResidue
CGLY521

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO C 602
ChainResidue
CASP482
CHOH764
DHIS20
DHOH265
CLYS481

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO F 601
ChainResidue
FGLY521
FLEU522
FLYS524
FHOH713

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO F 602
ChainResidue
FTYR536
FCYS573
FSER574
FPHE575
FALA576

site_idAC6
Number of Residues12
Detailsbinding site for Di-peptide GLY E 93 and LYS F 524
ChainResidue
DASN85
DCYS93
DASP127
DPRO128
DALA129
DHOH239
EGLY92
FLEU523
FSER525
FEDO601
FHOH707
FHOH785

Functional Information from PROSITE/UniProt
site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL
ChainResidueDetails
APHE82-LEU97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues306
DetailsDomain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsRegion: {"description":"Interaction with SUMO1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsSite: {"description":"Interaction with RANBP2"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Substrate binding"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"22509284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues6
DetailsMotif: {"description":"SUMO conjugation"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsSite: {"description":"Hydrophobic interaction with UBE2I","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15037602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues7
DetailsRegion: {"description":"Interaction with SUMO2 1","evidences":[{"source":"PubMed","id":"26524494","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues8
DetailsRegion: {"description":"Interaction with SUMO2 2","evidences":[{"source":"PubMed","id":"26524494","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues3
DetailsMotif: {"description":"PLRP","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

244693

PDB entries from 2025-11-12

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